The inhibition of monoamine oxidase by arylalkylhydrazines

Al, Green

doi:10.1042/bj0840217

Cited by 24 publications

(3 citation statements)

References 6 publications

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“…of preincubation (78). However, the effect of vetracin on the deamination of tyramine was the same when incubation was carried out in an atmosphere of oxygen or hydrogen as it was in air, and the replacement of air by nitrogen did not decrease the inhibition of vetracin (79). However, the effect of vetracin on the deamination of tyramine was the same when incubation was carried out in an atmosphere of oxygen or hydrogen as it was in air, and the replacement of air by nitrogen did not decrease the inhibition of vetracin (79).…”

Section: Hy Drazinesmentioning

confidence: 91%

Monoamine Oxidase Inhibitors

1972

Journal of Pharmaceutical Sciences

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Section: Hy Drazinesmentioning

confidence: 91%

Monoamine Oxidase Inhibitors

1972

Journal of Pharmaceutical Sciences

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“…Although several previous QSAR studies of M A 0 using a variety of different structural types of inhibitors have been reported (for early review see Fujita 1973), many of the compounds studied were capable of non-competitive inhibition and precautions were not taken to limit the studies to the initial competitive phase of the inhibition (Finkelstein et a1 1965;Martin et a1 1975). In other instances, the substrate employed has been capable of metabolism by both forms of the enzyme and the results preclude any consideration of the influence of the different forms of the enzyme (Lien et a1 1970;Green 1962). The present studies therefore report the preparation and testing of a series of nuclear-substituted pargyline derivatives as inhibitors of MAO-A and -B (using 5-HT and PEA, respectively, as substrates).…”

Section: Faculty Of Pharmacy University Of Toronto Toronto Ontariomentioning

confidence: 93%

Synthesis, Biological Evaluation and Quantitative Structure Activity Relationship Analysis of Nuclear-substituted Pargylines as Competitive Inhibitors of MAO-A and MAO-B

Ali

Robinson

1991

Journal of Pharmacy and Pharmacology

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A series of nuclear substituted derivatives of pargyline has been prepared and tested (under controlled conditions designed to measure the competitive component of the inhibition) as competitive inhibitors of MAO-A and -B. Adequate correlation of the biological data with the physiochemical constants of substituent groups was obtained only when the m- and p-substituted derivatives were considered separately. Due to the narrow range of activity displayed by the p-substituted derivates when inhibiting MAO-B, meaningful correlations were not found. However, the inhibition of MAO-B by the m-substituted derivatives required the inclusion of the Verloop L parameter for adequate correlation, suggesting that the inhibitor binding site of MAO-B is present within a cavity of more limited lateral dimensions than that present on the MAO-A surface. Inhibition of both MAO-A and -B demonstrated a parabolic relationship between inhibitory activity and pi. Whereas this parabolic relationship showed a maximal value for inhibition of MAO-A (mean pi o = 0.86), inhibition of MAO-B demonstrated a minimal value of pi (pi min = -0.5) i.e. the optimal value of pi for inhibition of MAO-B has not been achieved for this series of compounds but such would be greater than that demonstrated for MAO-A. The Hammett sigma function was important or significant only in the inhibition of MAO-A by the p-substituted derivatives.

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“…Monoamine oxidase activity was determined by the dinitrophenylhydrazine method (Green & Haughton, 1961). A suspension of guinea-pig liver mitochondria in sodium phosphate buffer (0.1 M, pH 7.4) was used as the enzyme source (Green, 1962). 0.4 ml.…”

mentioning

confidence: 99%